Complex of simian virus 40 large tumor antigen and 48,000-dalton host tumor antigen.
AUTOR(ES)
Greenspan, D S
RESUMO
Simian virus 40 large tumor antigen (T Ag) can be separated by sucrose gradient sedimentation into a rapidly sedimenting, maximally phosphorylated fraction and a slowly sedimenting, less phosphorylated fraction. The Mr 48,000 host tumor antigen (48,000 HTA, also called nonviral T Ag) is preferentially complexed with the maximally phosphorylated T Ag. Pulse-labeled T Ag sediments as a 5-6S monomer, whereas T Ag radiolabeled for progressively longer periods slowly increases in sedimentation coefficient to give a broad distribution between 5 S and greater than 28 S. Mutation in the viral A locus causes a decrease in T Ag phosphorylation and a marked decrease in 48,000 HTA binding, shifting the sedimentation coefficient of T Ag to the monomer value. The more highly phosphorylated T Ag also has the highest affinity for chromatin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=318999Documentos Relacionados
- Complex of simian virus 40 large-T antigen and host 53,000-molecular-weight protein in monkey cells.
- Specific in vitro adenylylation of the simian virus 40 large tumor antigen.
- Nature and origin of the RNA associated with simian virus 40 large tumor antigen.
- Production of simian virus 40 large tumor antigen in bacteria: altered DNA-binding specificity and dna-replication activity of underphosphorylated large tumor antigen.
- Association of a murine 53,000-dalton phosphoprotein with simian virus 40 large-T antigen in transformed cells.
